| + |
GSK3B | up-regulates activity 
phosphorylation
|
AHR |
0.253 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276666 |
Ser436 |
LRTKNGTsGKDSATT |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 34198826 |
A proposed model of GSK3β role on AHR function and degradation. AHR is phosphorylated by GSK3β in a p23-dependent manner in HeLa cells. This phosphorylation is required for optimal activation of the ligand-dependent AHR target gene transcription. After phosphorylation, AHR is K63-ubiquitinated and is targeted for the LC3-mediated selective autophagy. When the p23 content is compromised in HeLa cells, AHR is more prone to degradation via autophagy, bypassing the GSK3β phosphorylation of AHR. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276662 |
Ser440 |
NGTSGKDsATTSTLS |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 34198826 |
A proposed model of GSK3β role on AHR function and degradation. AHR is phosphorylated by GSK3β in a p23-dependent manner in HeLa cells. This phosphorylation is required for optimal activation of the ligand-dependent AHR target gene transcription. After phosphorylation, AHR is K63-ubiquitinated and is targeted for the LC3-mediated selective autophagy. When the p23 content is compromised in HeLa cells, AHR is more prone to degradation via autophagy, bypassing the GSK3β phosphorylation of AHR. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276664 |
Ser444 |
GKDSATTsTLSKDSL |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 34198826 |
A proposed model of GSK3β role on AHR function and degradation. AHR is phosphorylated by GSK3β in a p23-dependent manner in HeLa cells. This phosphorylation is required for optimal activation of the ligand-dependent AHR target gene transcription. After phosphorylation, AHR is K63-ubiquitinated and is targeted for the LC3-mediated selective autophagy. When the p23 content is compromised in HeLa cells, AHR is more prone to degradation via autophagy, bypassing the GSK3β phosphorylation of AHR. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276660 |
Ser689 |
SQEFPYKsEMDSMPY |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 34198826 |
A proposed model of GSK3β role on AHR function and degradation. AHR is phosphorylated by GSK3β in a p23-dependent manner in HeLa cells. This phosphorylation is required for optimal activation of the ligand-dependent AHR target gene transcription. After phosphorylation, AHR is K63-ubiquitinated and is targeted for the LC3-mediated selective autophagy. When the p23 content is compromised in HeLa cells, AHR is more prone to degradation via autophagy, bypassing the GSK3β phosphorylation of AHR. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276663 |
Ser693 |
PYKSEMDsMPYTQNF |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 34198826 |
A proposed model of GSK3β role on AHR function and degradation. AHR is phosphorylated by GSK3β in a p23-dependent manner in HeLa cells. This phosphorylation is required for optimal activation of the ligand-dependent AHR target gene transcription. After phosphorylation, AHR is K63-ubiquitinated and is targeted for the LC3-mediated selective autophagy. When the p23 content is compromised in HeLa cells, AHR is more prone to degradation via autophagy, bypassing the GSK3β phosphorylation of AHR. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276658 |
Ser723 |
ELDYPMGsFEPSPYP |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 34198826 |
A proposed model of GSK3β role on AHR function and degradation. AHR is phosphorylated by GSK3β in a p23-dependent manner in HeLa cells. This phosphorylation is required for optimal activation of the ligand-dependent AHR target gene transcription. After phosphorylation, AHR is K63-ubiquitinated and is targeted for the LC3-mediated selective autophagy. When the p23 content is compromised in HeLa cells, AHR is more prone to degradation via autophagy, bypassing the GSK3β phosphorylation of AHR. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276659 |
Ser727 |
PMGSFEPsPYPTTSS |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 34198826 |
A proposed model of GSK3β role on AHR function and degradation. AHR is phosphorylated by GSK3β in a p23-dependent manner in HeLa cells. This phosphorylation is required for optimal activation of the ligand-dependent AHR target gene transcription. After phosphorylation, AHR is K63-ubiquitinated and is targeted for the LC3-mediated selective autophagy. When the p23 content is compromised in HeLa cells, AHR is more prone to degradation via autophagy, bypassing the GSK3β phosphorylation of AHR. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276661 |
Thr697 |
EMDSMPYtQNFISCN |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 34198826 |
A proposed model of GSK3β role on AHR function and degradation. AHR is phosphorylated by GSK3β in a p23-dependent manner in HeLa cells. This phosphorylation is required for optimal activation of the ligand-dependent AHR target gene transcription. After phosphorylation, AHR is K63-ubiquitinated and is targeted for the LC3-mediated selective autophagy. When the p23 content is compromised in HeLa cells, AHR is more prone to degradation via autophagy, bypassing the GSK3β phosphorylation of AHR. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276665 |
Thr731 |
FEPSPYPtTSSLEDF |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 34198826 |
A proposed model of GSK3β role on AHR function and degradation. AHR is phosphorylated by GSK3β in a p23-dependent manner in HeLa cells. This phosphorylation is required for optimal activation of the ligand-dependent AHR target gene transcription. After phosphorylation, AHR is K63-ubiquitinated and is targeted for the LC3-mediated selective autophagy. When the p23 content is compromised in HeLa cells, AHR is more prone to degradation via autophagy, bypassing the GSK3β phosphorylation of AHR. |
|
| Publications: |
9 |
Organism: |
Homo Sapiens |
| + |
4,4'-sulfonyldiphenol | up-regulates activity
chemical activation
|
AHR |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268736 |
|
|
in vitro |
|
| pmid |
sentence |
| 31995776 |
This study investigated the endocrine-disrupting activity of BPA, BPF, and BPS alone or as a mixture and the agonistic and antagonistic activity of the BPs using an in vitro bioassay to detect ER-, AR-, and AhR-mediated activity.In our study, BPs showed AhR agonist activity only at the highest concentrations, and the mixture did not differ from the single BPs. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
AHR | up-regulates quantity by expression
transcriptional regulation
|
CYP1A1 |
0.673 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-259909 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17012224 |
Kaempferol proved to be capable of inhibiting binding of agonist and agonist-induced formation of the AHR/ARNT DNA-binding complex and upregulation of the AHR target gene, CYP1A1. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253639 |
|
|
in vitro |
|
| pmid |
sentence |
| 9865727 |
Resveratrol inhibits transcription of CYP1A1 in vitro by preventing activation of the aryl hydrocarbon receptor|These data demonstrate that resveratrol inhibits CYP1A1 expression in vitro, and that it does this by preventing the binding of the AHR to promoter sequences that regulate CYP1A1 transcription. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens, In Vitro |
| + |
AHR | up-regulates quantity by expression 
transcriptional regulation
|
UGT1A1 |
0.416 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253734 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18172616 |
Human UDP-glucuronosyltransferase (UGT)1A1 is a critical enzyme responsible for detoxification and metabolism of endogenous and exogenous lipophilic compounds, such as potentially neurotoxic bilirubin and the anticancer drug irinotecan SN-38, via conjugation with glucuronic acid. A 290-bp distal enhancer module, phenobarbital-responsive enhancer module of UGT1A1 (gtPBREM), fully accounts for constitutive androstane receptor (CAR)-, pregnane X receptor (PXR)-, glucocorticoid receptor (GR)-, and aryl hydrocarbon receptor (AhR)-mediated activation of the UGT1A1 gene. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
bisphenol A | up-regulates activity
chemical activation
|
AHR |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268735 |
|
|
in vitro |
|
| pmid |
sentence |
| 31995776 |
This study investigated the endocrine-disrupting activity of BPA, BPF, and BPS alone or as a mixture and the agonistic and antagonistic activity of the BPs using an in vitro bioassay to detect ER-, AR-, and AhR-mediated activity.In our study, BPs showed AhR agonist activity only at the highest concentrations, and the mixture did not differ from the single BPs. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
AHR | form complex 
binding
|
AHR-ARNT |
0.744 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-240817 |
|
|
in vitro |
|
| pmid |
sentence |
| 9020169 |
SIM1 and SIM2, and the mammalian aryl hydrocarbon receptor (AHR) and aryl hydrocarbon receptor nuclear translocator (ARNT) proteins are members of the basic-helix-loop-helix·PAS family of transcription factors. In the yeast two-hybrid system, we demonstrate strong constitutive interaction of ARNT with SIM1 and SIM2 and fully ligand-dependent interaction of ARNT with AHR. SIM1 inhibits binding of the AHR·ARNT dimer to the xenobiotic response element in vitro Introduction of SIM1 into hepatoma cells inhibits transcriptional transactivation by the endogenous AHR·ARNT dimer. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
bisphenol F | up-regulates activity
chemical activation
|
AHR |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268737 |
|
|
in vitro |
|
| pmid |
sentence |
| 31995776 |
This study investigated the endocrine-disrupting activity of BPA, BPF, and BPS alone or as a mixture and the agonistic and antagonistic activity of the BPs using an in vitro bioassay to detect ER-, AR-, and AhR-mediated activity.In our study, BPs showed AhR agonist activity only at the highest concentrations, and the mixture did not differ from the single BPs. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
resveratrol | down-regulates activity 
chemical inhibition
|
AHR |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253640 |
|
|
in vitro |
|
| pmid |
sentence |
| 9865727 |
Resveratrol inhibits transcription of CYP1A1 in vitro by preventing activation of the aryl hydrocarbon receptor|These data demonstrate that resveratrol inhibits CYP1A1 expression in vitro, and that it does this by preventing the binding of the AHR to promoter sequences that regulate CYP1A1 transcription. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
OSM | up-regulates quantity by expression
transcriptional regulation
|
AHR |
0.349 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-202963 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 24127753 |
The il-6-type cytokine oncostatin m induces ahr expression in a stat3-ependent manner in human hepg2 hepatoma cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AHR | up-regulates quantity by expression
transcriptional regulation
|
CYP1B1 |
0.505 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253733 |
|
|
Homo sapiens |
Prostate Cancer Cell Line |
| pmid |
sentence |
| 16115918 |
Expressions of CYP1B1 mRNA and protein were increased in prostate cancer. The aryl hydrocarbon receptor (AhR)/AhR nuclear translocator (ARNT) heterodimer complex activates gene transcription by binding to the DREs of CYP1B1. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Monobutylphthalate | up-regulates activity
chemical activation
|
AHR |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268791 |
|
|
in vitro |
|
| pmid |
sentence |
| 25081364 |
BBP affected hepatocellular carcinoma progression through the aryl hydrocarbon receptor (AhR) and that benzyl butyl phthalate (BBP) stimulated AhR at the cell surface, which then interacted with G proteins and triggered a downstream signaling cascade. BBP activated AhR through a nongenomic action involving G-protein signaling rather than the classical genomic AhR action. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
AHR | up-regulates quantity by expression
transcriptional regulation
|
CYP1B1 |
0.505 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253642 |
|
|
|
|
| pmid |
sentence |
| 17012224 |
The formation of the AHR/ARNT dimerization complex converts the AHR into a high affinity DNA-binding form that recognizes specific DNA recognition sites termed DREs. In this manner, the agonist activated AHR upregulates a battery of target genes, including those involved in the metabolism of chemical carcinogens, such as CYP1A1 and CYP1B1 . |
|
| Publications: |
1 |
3.0
AHR
- 
- 